2v9f
From Proteopedia
|
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A-K248W-A273S)
Overview
The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface. Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore the number of required mutations. Some of the proteins needed only a single side-chain alteration in order to associate to a higher-order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures.
About this Structure
2V9F is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Rhamnulose-1-phosphate aldolase, with EC number 4.1.2.19 Known structural/functional Sites: , , , , , and . Full crystallographic information is available from OCA.
Reference
Designed protein-protein association., Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE, Science. 2008 Jan 11;319(5860):206-9. PMID:18187656
Page seeded by OCA on Thu Feb 21 18:54:15 2008
Categories: Escherichia coli | Rhamnulose-1-phosphate aldolase | Single protein | Grueninger, D. | Schulz, G E. | ACT | ZN | 2-ketose degradation | Aggregation | Aldolase | Class ii | Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetoneph bacterial l-rhamnose metabolism | Cytoplasm | Entropy index | Fibrillation | Interface design | Lyase | Metal-binding | Oligomerization | Protein engineering | Protein-protein interface | Rare sugar | Rhamnose metabolism | Surface mutation | Zinc | Zinc enzyme
